Electrophoretic Heterogeneity of the Polypeptide Chains of Human G-Myeloma Proteins

Abstract
The light and heavy polypeptide chains derived from human Gmyeloma proteins are electrophoretically heterogeneous as judged by disc electrophoresis of the polypeptide chains in urea-acrylamide gels. Individual myeloma proteins contained as many as eight light-chain and nine heavy-chain components.